纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | FMO2 |
Uniprot No | P31512 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-558aa |
氨基酸序列 | MAKKVAVIGAGVSGLSSIKCCVDEDLEPTCFERSDDIGGLWKFTESSKDGMTRVYKSLVTNVCKEMSCYSDFPFHEDYPNFMNHEKFWDYLQEFAEHFDLLKYIQFKTTVCSITKRPDFSETGQWDVVTETEGKQNRAVFDAVMVCTGHFLNPHLPLEAFPGIHKFKGQILHSQEYKIPEGFQGKRVLVIGLGNTGGDIAVELSRTAAQVLLSTRTGTWVLGRSSDWGYPYNMMVTRRCCSFIAQVLPSRFLNWIQERKLNKRFNHEDYGLSITKGKKAKFIVNDELPNCILCGAITMKTSVIEFTETSAVFEDGTVEENIDVVIFTTGYTFSFPFFEEPLKSLCTKKIFLYKQVFPLNLERATLAIIGLIGLKGSILSGTELQARWVTRVFKGLCKIPPSQKLMMEATEKEQLIKRGVFKDTSKDKFDYIAYMDDIAACIGTKPSIPLLFLKDPRLAWEVFFGPCTPYQYRLMGPGKWDGARNAILTQWDRTLKPLKTRIVPDSSKPASMSHYLKAWGAPVLLASLLLICKSSLFLKLVRDKLQDRMSPYLVSLWRG |
预测分子量 | 63,3 kDa |
蛋白标签 | His tag N-Terminus |
缓冲液 | PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300. |
稳定性 & 储存条件 | Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months. |
复溶 | Always centrifuge tubes before opening.Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles. |
以下是关于FMO2重组蛋白的3篇参考文献的简要信息:
1. **文献名称**:*"Expression and Characterization of Recombinant Human Flavin-Containing Monooxygenase 2 (FMO2)"*
**作者**:Cashman, J.R. 等
**摘要**:该研究报道了在哺乳动物细胞中重组表达人源FMO2蛋白的方法,分析了其对特定含硫底物的催化活性,揭示了其与FMO家族其他成员的代谢差异。
2. **文献名称**:*"Optimization of FMO2 Recombinant Protein Production in Escherichia coli for Functional Studies"*
**作者**:Hernandez, D. 等
**摘要**:通过优化大肠杆菌表达系统(如密码子选择、诱导条件),成功获得高活性可溶的FMO2重组蛋白,并验证其在体外代谢模型中的应用潜力。
3. **文献名称**:*"Functional Impact of FMO2 Genetic Variants on Recombinant Protein Activity"*
**作者**:Krueger, S.K. 等
**摘要**:研究比较了不同FMO2基因多态性(如Q472X突变)对重组蛋白表达及酶活性的影响,揭示了某些变异可能导致功能缺失或代谢能力下降。
(注:以上文献信息为示例性概括,实际研究需通过学术数据库检索确认具体细节。)
Flavin-containing Monooxygenase 2 (FMO2) is a member of the FMO enzyme family, which catalyzes oxygen- and NADPH-dependent oxidation of xenobiotics, including drugs, environmental toxins, and endogenous metabolites. FMO2 is primarily expressed in the lungs, kidneys, and liver across species, though its activity varies significantly due to genetic polymorphisms. In humans, the majority of the population carries a truncated, non-functional FMO2 allele (FMO2*2), resulting in loss-of-function due to a premature stop codon. Functional full-length FMO2 (FMO2*1) is rare, found predominantly in individuals of African or Hispanic descent. This genetic variation impacts drug metabolism and personalized medicine approaches.
Recombinant FMO2 protein is engineered to study its enzymatic mechanisms, substrate specificity, and role in detoxification pathways. Produced via heterologous expression systems (e.g., E. coli, insect cells, or mammalian cells), it enables controlled in vitro analysis without interference from other FMO isoforms like FMO3. the dominant hepatic form. Researchers use recombinant FMO2 to explore its unique ability to metabolize bulky substrates, including certain therapeutics (e.g., itopride) and sulfur/nitrogen-containing compounds. Its role in bioactivating prodrugs or generating toxic metabolites is also a focus, particularly in lung-related toxicology.
Studies on recombinant FMO2 have clarified its structural features, including the FAD-binding domain and catalytic sites, aiding drug design and toxicity prediction. Additionally, it serves as a tool to investigate interethnic differences in drug response linked to FMO2 polymorphisms. Ongoing research aims to harness its potential in targeted therapies and improve understanding of its physiological roles beyond xenobiotic metabolism, such as in lipid homeostasis and disease pathogenesis.
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